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METALLOPROTEASES IN TRYPANOSOMA RANGELI-INFECTED RHODNIUS PROLIXUS
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Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Bioquímica e Biologia Molecular. Rio de Janeiro, RJ, Brasil.
Abstract
Protease activities in the haemolymph and fat body in a bloodsucking insect, Rhodnius prolixus,
infected with Trypanosoma rangeli, were investigated. After SDS-polyacrylamide gel electrophoresis
containing gelatin as substrate, analysis of zymograms performed on samples of different tissues of
controls and insects inoculated or orally infected with short or long epimastigotes of T. rangeli, demonstrated distinct patterns of protease activities: (i) proteases were detected in the haemolymph of insects
which were fed on, or inoculated with, short epimastigotes of T. rangeli (39 kDa and 33 kDa, respectively), but they were not observed in the fat body taken from these insects; (ii) protease was also
presented in the fat bodies derived from naive insects or controls inoculated with sterile phosphatesaline buffer (49 kDa), but it was not detected in the haemolymph of these insects; (iii) no protease
activity was observed in both haemolymph and fat bodies taken from insects inoculated with, or fed on,
long epimastigotes of T. rangeli. Furthermore, in short epimastigotes of T. rangeli extracts, three bands
of the protease activities with apparent molecular weights of 297, 198 and 95 kDa were detected while
long epimastigotes preparation presented only two bands of protease activities with molecular weights
of 297 and 198 kDa. The proteases from the insect infected with T. rangeli and controls belong to the
class of either metalloproteases or metal-activated enzymes since they are inhibited by 1,10-
phenanthroline. The significance of these proteases in the insects infected with short epimastigotes of
T. rangeli is discussed in relation to the success of the establishment of infection of these parasites in its
vector, R. prolixus.
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